Inhibition of -amylase digestion by a Lonicera caerulea berry polyphenol starch complex revealed via multi-spectroscopic and molecular dynamics analyses

Polyphenol-starch complexes exhibit synergistic and beneficial effects on both polyphenols and resistant starches. This study evaluates the inhibitory effects and mechanisms of alpha-amylase on a Lonicera caerulea berry polyphenol-wheat starch (LPWS) complex following high hydrostatic pressure treatments of 400 MPa for 30 min and 600 MPa for 30 min. The IC50 values for alpha-amylase inhibition by the complex were 3.61 +/- 0.10 mg/mL and 3.42 +/- 0.08 mg/mL at a 10 % (w/w) polyphenol content. This interaction was further supported by Fouriertransform infrared spectroscopy and circular dichroism, which confirmed that the alpha helix component of the secondary structure of alpha-amylase was reduced due to the complex. Multifluorescence spectroscopy revealed that the complex induces changes in the microenvironment of fluorophores surrounding the alpha-amylase active site. Molecular dynamics simulations and molecular docking revealed that the active site of amylose within the complex becomes enveloped in polyphenol clusters. This wrapping effect reduced the hydrogen bonds between amylose and alpha-amylase, decreasing from 16 groups to just one group. In summary, the LPWS complex represents a low -digestible carbohydrate food source, thus laying the groundwork for the research and development of functional foods aimed at postprandial hypoglycemic effects.